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Structural and spectroscopic insights into BolA-glutaredoxin complexes.

Thomas Roret1, Pascale Tsan1, Jérémy Couturier2

  • 1From the Université de Lorraine and CNRS, UMR 7036 CRM2, BioMod group, 54506 Vandœuvre-lès-Nancy, France.

The Journal of Biological Chemistry
|July 12, 2014
PubMed
Summary

Arabidopsis BolA proteins, involved in stress response and iron metabolism, form complexes with glutaredoxins. Structural studies reveal how cysteine or histidine in BolA proteins coordinate iron-sulfur clusters, impacting their function.

Keywords:
BolAComplexesGlutaredoxinGlutathioneIron MetabolismIron-Sulfur ProteinRedox RegulationThiol

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Area of Science:

  • Plant molecular biology
  • Protein structure and function
  • Iron-sulfur cluster metabolism

Background:

  • BolA proteins are known stress-responsive transcriptional regulators with roles in iron metabolism.
  • BolA proteins can form complexes with monothiol glutaredoxins (Grx), but their structural basis is unclear.
  • Structural variations in BolA proteins, particularly the variable [H/C] loop, suggest functional diversity.

Purpose of the Study:

  • To elucidate the structural basis of BolA-glutaredoxin complex formation.
  • To investigate the role of the variable [H/C] loop in BolA protein function and iron metabolism.
  • To understand the coordination of [2Fe-2S] clusters within BolA-Grx complexes.

Main Methods:

  • X-ray crystallography was used to solve three structures of Arabidopsis thaliana BolA proteins.
  • Three-dimensional modeling and spectroscopic analyses were performed on Arabidopsis thaliana GrxS14-BolA1 holo-heterodimer.
  • Nuclear Magnetic Resonance (NMR) interaction experiments were conducted using BolA apoproteins.

Main Results:

  • Structural differences in BolA proteins are primarily due to the variable [H/C] loop, containing a cysteine or histidine residue.
  • Evidence for the coordination of a Rieske-type [2Fe-2S] cluster in BolA_H group proteins was found, with cysteine potentially substituting histidine in BolA_C group.
  • NMR experiments revealed distinct heterodimer formation involving the nucleic acid binding site of BolA and the C-terminal tail of Grx.

Conclusions:

  • The variable [H/C] loop of BolA proteins plays a critical role in coordinating iron-sulfur clusters.
  • BolA proteins can form at least two distinct types of heterodimers with glutaredoxins, suggesting diverse functional roles.
  • These findings provide structural insights into the participation of BolA proteins in iron metabolism and stress response pathways.